4DZB

Mucosal-associated invariant T cell receptor, Valpha7.2Jalpha33-Vbeta2

Summary for 4DZB

• Entry DOI: 10.2210/pdb4dzb/pdb
• Descriptor: Valpha7.2-Jalpha33 (MAIT T cell receptor), Vbeta2 (MAIT T cell receptor) (3 entities in total)
• Functional Keywords: mait t cell receptor, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 50322.93

Authors

Patel, O.,Rossjohn, J. (deposition date: 2012-03-01, release date: 2012-03-28, Last modification date: 2024-11-27)

Primary citation

Reantragoon, R.,Kjer-Nielsen, L.,Patel, O.,Chen, Z.,Illing, P.T.,Bhati, M.,Kostenko, L.,Bharadwaj, M.,Meehan, B.,Hansen, T.H.,Godfrey, D.I.,Rossjohn, J.,McCluskey, J.
Structural insight into MR1-mediated recognition of the mucosal associated invariant T cell receptor.
J.Exp.Med., 209:761-774, 2012

PubMed Abstract: Mucosal-associated invariant T (MAIT) cells express a semiinvariant αβ T cell receptor (TCR) that binds MHC class I-like molecule (MR1). However, the molecular basis for MAIT TCR recognition by MR1 is unknown. In this study, we present the crystal structure of a human Vα7.2Jα33-Vβ2 MAIT TCR. Mutagenesis revealed highly conserved requirements for the MAIT TCR-MR1 interaction across different human MAIT TCRs stimulated by distinct microbial sources. Individual residues within the MAIT TCR β chain were dispensable for the interaction with MR1, whereas the invariant MAIT TCR α chain controlled specificity through a small number of residues, which are conserved across species and located within the Vα-Jα regions. Mutagenesis of MR1 showed that only two residues, which were centrally positioned and on opposing sides of the antigen-binding cleft of MR1, were essential for MAIT cell activation. The mutagenesis data are consistent with a centrally located MAIT TCR-MR1 docking that was dominated by the α chain of the MAIT TCR. This candidate docking mode contrasts with that of the NKT TCR-CD1d-antigen interaction, in which both the α and β chain of the NKT TCR is required for ligation above the F'-pocket of CD1d.

PubMed: 22412157
DOI: 10.1084/jem.20112095

Experimental method

X-RAY DIFFRACTION (1.7 Å)